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1401 results for "E1-ClipTip"

1401 Results for: "E1-ClipTip"

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Anti-ADGRE1 Rat Monoclonal Antibody (PerCP (Peridinin-Chlorophyll Protein Complex)-Cy5.5®) [clone: BM8.1]

Anti-ADGRE1 Rat Monoclonal Antibody (PerCP (Peridinin-Chlorophyll Protein Complex)-Cy5.5®) [clone: BM8.1]

Supplier: Tonbo Biosciences

The BM8.1 antibody is specific for mouse F4/80 antigen, a 125 kDa transmembrane protein widely expressed by members of the mononuclear phagocyte system and considered to be a key marker for mature macrophage cells. F4/80 is differentially expressed during myeloid cell development, and may be regulated by certain cytokines within the tissue microenvironment. Other cell types shown to express this antigen include Langerhans cells, Kupffer cells and dendritic cell subsets. BM8.1 is widely used together with antibodies to CD115 (c-fms), CD11b and CD11c to identify myeloid / macrophage cells by flow cytometry.

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Bis(2-hydroxyethyl)amino tris(hydroxymethyl)methane (BIS-TRIS) ≥99%, white powder, Cell Culture Grade

Supplier: MP Biomedicals

Bis-Tris is a zwitterionic buffer; an amine buffer similar to Tris Hydrochloric acid that exhibits only a very small shift in dissociation constant with respect to temperature. It is structurally analogous to the the Good buffers that were developed to provide buffers in the pH range of 6.15 - 8.35 for wide applicability to biochemical studies.

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Anti-ADGRE1 Rat Monoclonal Antibody (APC (Allophycocyanin)) [clone: BM8.1]

Anti-ADGRE1 Rat Monoclonal Antibody (APC (Allophycocyanin)) [clone: BM8.1]

Supplier: Tonbo Biosciences

The BM8.1 antibody is specific for mouse F4/80 antigen, a 125 kDa transmembrane protein widely expressed by members of the mononuclear phagocyte system and considered to be a key marker for mature macrophage cells. F4/80 is differentially expressed during myeloid cell development, and may be regulated by certain cytokines within the tissue microenvironment. Other cell types shown to express this antigen include Langerhans cells, Kupffer cells and dendritic cell subsets. BM8.1 is widely used together with antibodies to CD115 (c-fms), CD11b and CD11c to identify myeloid / macrophage cells by flow cytometry.

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Bovine Aprotinin (from Lung), MP Biomedicals

Supplier: MP Biomedicals

Aprotinin is found in bovine lymph nodes, lung, parotid gland, spleen, liver, pancreas, seminal vesicles, thyroid gland, kidney, mucous membranes of the trachea and esophagus, ovaries, heart, posterior pituitary and cartilage. It is a serine protease inhibitor which is reactive against trypsin, chymotrypsin, plasmatic and glandular kininogenases, plasmin, kallkrein, urokinase, clotting factor XIIa, protein C, proteinases of the complement system, leukocyte and tissue proteinases. It does not inhibit thrombin. Aprotinin works by blocking the active sites of enzymes. Binding is reversible with most aprotinin-protease complexes dissociating at pH > 10 or < 3.

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Human Recombinant Yin and Yang 1 (from E. coli)

Supplier: Prosci

Transcriptional repressor protein YY1(YY1)contains 4 C2H2-type zinc fingers and belongs to the YY transcription factor family. Multifunctional transcription factor exhibits positive and negative control on a large number of cellular and viral genes by binding to sites overlapping the transcription start site. The effect on transcription regulation of the protein is depending upon the context in which it binds and diverse mechanisms of action include direct activation or repression, indirect activation or repression via cofactor recruitment, or activation or repression by disruption of binding sites or conformational DNA changes. Its activity is regulated by transcription factors and cytoplasmic proteins that have been shown to abrogate or completely inhibit YY1-mediated activation or repression.

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Tritirachium album Proteinase K, MP Biomedicals

Supplier: MP Biomedicals

Proteinase K is a highly active stable endopeptidase with a broad spectrum of action was isolated by E. Merk's Darmstadt Biochemical Research Department in 1970 from a culture filtrate of the fungus, Tritirachium album Limber. This fungus is able to grow on Keratin (e.g., wool, horn particles) as the sole source of carbon and nitrogen. The isolated protease was, therefore, given the K designation.

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Ubiquitinylation Kit, Enzo Life Sciences

Ubiquitinylation Kit, Enzo Life Sciences

Supplier: Enzo Life Sciences

Versatile tool for generation of ubiquitin-E2 thioesters.

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DetectX® Estrone ELISA Kits

Supplier: ARBOR ASSAYS MS

The Estrone ELISA Kit from Arbor Assays is a competitive immunoassay designed for the quantitative measurement of estrone in dried fecal extracts, urine, and tissue culture media. Utilizing a goat anti-rabbit IgG-coated plate, a rabbit polyclonal antibody, and an estrone-peroxidase conjugate, this assay provides colorimetric detection at 450 nm. With a sensitivity of 22.4 pg/ml, the kit enables accurate and reproducible estrone measurement in 2.5 hours. This assay is ideal for research in reproductive physiology, endocrinology, and related fields, offering a reliable and efficient method for estrone quantification.

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Bovine Aprotinin (from Lung), MP Biomedicals

Supplier: MP Biomedicals

Aprotinin is a single chain polypeptide (58 amino-acids) crosslinked by three disulfide bridges, showing competitive and reversible inhibiton of proteolytic and esterolytic activity. Aprotinin forms stable complexes with, and blocks the active sites of serine protease enzymes. It is found in bovine lymph nodes, lung, parotid gland, spleen, liver, pancreas, seminal vesicles, thyroid gland, kidney, mucous membranes of the trachea and esophagus, ovaries, heart, posterior pituitary and cartilage.

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L(-)-Tyrosine, off-white powder cell culture reagent

Supplier: MP Biomedicals

Storage: Store at room temperature (15-30 °C)
L-Tyrosine is one of the three aromatic amino acids, and is formed from the hydroxylation of phenylalanine.
L-Tyrosine is used in cell culture media and is a component of MEM amino acids solution. L-Tyrosine has been used in a cell culture study of the amino acid transport system b0,+ in epithelial cells isolated from chicken jejunum.

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Concanavalin A (from Jackbean), MP Biomedicals

Supplier: MP Biomedicals

Pure Canavalia ensiformis lectin (Con A) from Jackbean.

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Folic acid ≥95%, orange powder cell culture reagent

Supplier: MP Biomedicals

Storage: Store at Room Temperature (15-30 °C). Protect from light.
Folic acid, also known as folate, is a B vitamin that can be found in a variety of fruits and vegetables. It can also be chemically synthesized. Folate, a watersoluble vitamin, helps the body form red blood cells and aids in the formation of genetic material within every body cell. Folic Acid is a hematopoietic vitamin present, free or combined with one or more additional molecules of L- (+)-glutamic acid, in liver, kidney, mushrooms, spinach, yeast, green leaves, and grasses.
A nutritional delivery form of folate. Folic acid and its derivatives are essential mediators of one-carbon metabolism within cells.

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ABTS (Diammonium 2,2'-azinobis[3-ethyl-2,3-dihydrobenzothiazole-6-sulfonate]), light green powder

ABTS (Diammonium 2,2'-azinobis[3-ethyl-2,3-dihydrobenzothiazole-6-sulfonate]), light green powder

Supplier: MP Biomedicals

2,2-Azino-bis-(3-ethyl-benzthiazoline-6-sulfonic acid) (ABTS) has been used as a chromogenic substrate for horseradish peroxidase (HRP), both in general activity assays and in ELISA applications. Activity of HRP using ABTS appears about four-fold higher than using pyrogallol. It is mainly used as a substrate in sensitive peroxidase assays.
2,2′-Azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) is a peroxidase substrate suitable for use in ELISA procedures. This substrate produces a soluble end product that is green in color and can be read spectrophotometrically at 405 nm. The reaction may be stopped with 1% sodium dodecyl sulfate (SDS). Recommended for ELISA (microwell) procedures, not recommended for membrane applications.

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Acetyl Coenzyme A Trilithium Salt Trihydrate, MP Biomedicals

Supplier: MP Biomedicals

Acetyl-CoA is produced via beta-oxidation of fatty acids, via the metabolism of carbohydrates - glucose 6-phosphate to pyruvate to acetyl-CoA and via the catabolism of amino acids. Acetyl-CoA has a number of metabolic opportunities. It is metabolized in the tricarboxylic acid cycle to produce carbon dioxide, water and energy.

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Adenosine-5'-triphosphate disodium salt (ATP disodium salt) trihydrate ≥99%, white powder cell culture reagent

Supplier: MP Biomedicals

Storage: -20 °C.
Adenosine 5'-triphosphate (ATP) and its phosphate bonds are the basic components of energy exchange in many biological systems.
Adenosine 5'-triphosphate (ATP) is a central component of energy storage and metabolism in vivo. ATP is used in many cellular processes, respiration, biosynthetic reactions, motility, and cell division. ATP is a substrate of many kinases involved in cell signaling and of adenylate cyclase(s) that produce the second messenger cAMP. ATP provides the metabolic energy to drive metabolic pumps. ATP serves as a coenzyme in a wide array of enzymatic reactions.
P2 purinergic agonist; increases activity of Ca2+-activated K+ channels; substrate for ATP-dependent enzyme systems.

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Ficin, MP Biomedicals

Supplier: MP Biomedicals

Ficin is a purified ficin preparation which is extracted from the latex of the fig tree Ficus glabrata. Ficin is classified as a thiol protease. Ficin hydrolyses the peptide bonds where the carbonyl group is from phenylalanine or tyrosine. When used in conjunction with other plants proteases, papain or bromelain, a synergistic effect may be observed. Immobilized Ficin was specifically designed for cleavage of mouse IgG1 into F(ab')2 or Fab fragments.The immobilization of ficin enhances stability against denaturation, heat and autolysis. Immobilization also eliminates any potential for antibody-enzyme adducts that cause continued sample digestion.

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Glucose Oxidase (from Aspergillus niger), MP Biomedicals

Supplier: MP Biomedicals

Glucose oxidase is an FAD-containing glycoprotein. The enzyme is specific for β-D-glucose. O can be replaced by hydrogen acceptors such as 2,6-dichlorophenol indophenol. Glucose oxidase from Aspergillus niger is a dimer consisting of 2 equal subunits with a molecular mass of 80 kDa each. Each subunit contains one flavin adenine dinulceotide moiety and one iron. The enzyme is a glycoprotein containing ~16% neutral sugar and 2% amino sugars. The enzyme also contains 3 cysteine residues and 8 potential sites for N-linked glycosylation. Glucose oxidase is capable of oxidizing D-aldohexoses, monodeoxy-D-glucoses, and methyl-D-glucoses at varying rates. Glucose oxidase does not require any activators, but it is inhibited by Ag+, Hg2+, Cu2+, phenylmercuric acetate, and p-chloromercuribenzoate. It is not inhibited by the nonmetallic SH reagents: N-ethylmaleimide, iodoacetate, and iodoacetamide.

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Bovine Deoxyribonuclease I (from Pancreas), MP Biomedicals

Supplier: MP Biomedicals

Deoxyribonuclease from beef pancreas, DNase I, was first crystallized by Kunitz. It is an endonuclease which splits phosphodiester linkages, preferentially adjacent to a pyrimidine nucleotide yielding 5'-phosphate terminated polynucleotides with a free hydroxyl group on position 3'. The average chain of limit digest is a tetranucleotide. DNase I acts upon single chain DNA, and upon double-stranded DNA and chromatin. In the latter case, although histones restrict susceptibility to nuclease action, over a period of time nearly all chromatin DNA is acted upon. According to Mirsky and Silverman, this could result from the looseness of histone attachment to DNA. They found that lysine-rich histones more effectively block DNase access to DNA than arginine-rich histones. Billing and Bonner suggest that DNase attacks the histone-free strand of chromatin DNA. Schmidt, et. al.indicate that hydrolysis of the histone-free region of DNA strands accounts for the initial rapid action of the enzyme on chromatin. Bollum reports degradation of synthetic homopolymer complexes by DNase I. The intracellular functions of the enzyme are probably controlled by a DNase inhibitor, which according to Lazarides and Lindberg is actin.

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Folic acid ≥95%, orange powder

Supplier: MP Biomedicals

Folic acid, also known as folate, is a B vitamin that can be found in a variety of fruits and vegetables. It can also be chemically synthesized. Folate, a watersoluble vitamin, helps the body form red blood cells and aids in the formation of genetic material within every body cell. This product exhibits metal binding properties. Hematopoietic vitamin present, free or combined with one or more additional molecules of L-(+)-glutamic acid, in liver, kidney, mushrooms, spinach, yeast, green leaves, and grasses.
Folic acid (Vitamin B9 and folate) is essential to numerous bodily functions. The human body needs folate to synthesize DNA, repair DNA, and methylate DNA as well as to act as a cofactor in certain biological reactions. It is especially important in aiding rapid cell division and growth, such as in infancy and pregnancy.
Folic acid (FA) and dihydrofolic acid (FAH2) are substrates of dihydrofolate reductase(s) which reduce them to tetrahydrofolate (THF), which in turn supports ‘one carbon’ transfer. Tetrahydrofolates are required for de novo synthesis of purines, thymidylic acid and various amino acids and for post-translational methylation (epigenetics).
Very slightly soluble in cold water (0.0016 mg/mL at 25 °C), soluble to about 1% in boiling water. Slightly soluble in methanol, appreciably less soluble in ethanol and butanol. Insoluble in acetone, chloroform, ether, benzene. Relatively soluble in acetic acid, phenol, pyridine, solutions of alkali hydroxides and carbonates. Soluble in hot dilute HCl and H2SO4.

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β-Nicotinamide adenine dinucleotid, oxidised form (NAD, oxidised form) ≥98%, white powder cell culture reagent

Supplier: MP Biomedicals

Storage: -20°C, desiccate
This is an ultrapure NAD, chromatographically purified to remove trace inhibitors.
β-NAD, a pyridine nucleotide and biologically active form of nicotinic acid, is a coenzyme necessary for the catalytic reaction of certain enzymes. It occurs in living cells primarily in the oxidized state. Serves as a coenzyme of the dehydrogenases, especially in the dehydrogenation of primary and secondary alcohols. NAD usually acts as a hydrogen acceptor, forming NADH which then serves as a hydrogen donor in the respiratory chain.
Many metabolites and enzymes of biological interest are present in tissues at low concentrations. With the use of β-NAD as a catalyst intermediate and several enzymes in a multistep system, known as enzyme cycling, much greater sensitivity for detection of these components is achieved. The reduced form, β-NADH, is fluorescent whereas β-NAD is not. This difference in fluorescence provides a sensitive fluorescent measurement of the oxidized or reduced pyridine nucleotides at concentrations down to 10-7 M.
Electron acceptor. β-NAD is a carrier for hydride ion, forming b-NADH. Hydride ion is enzymatically removed from a substrate molecule by the action of dehydrogenases such as malic dehydrogenase and lactic dehydrogenase. Such enzymes catalyze the reversible transfer of a hydride ion from malate or lactate to b-NAD to form the reduced product, b-NADH. Unlike b-NAD which has no absorbance at 340 nm, b-NADH absorbs at 340 nm (EmM = 6.22). The increase in absorbance at 340 nm with the formation of b-NADH is the basis for measurement of activity of many enzymes.

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ß-Nicotinamide adenine dinucleotide phosphate (NADP-Na2, oxidized form) ≥98%, white powder

Supplier: MP Biomedicals

β-NADP is a coenzyme necessary for the alcoholic fermentation of glucose and the oxidative dehydrogenation of other substances. It occurs widely in living tissue, especially in the liver. Nicotinic acid can be converted to nicotinamide in the body and, in this form, is found as a component of two oxidation-reduction coenzymes: nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP). The nicotinamide portion of the coenzyme transfers hydrogens by alternating between oxidized quaternary nitrogen and a reduced tertiary nitrogen. NADP is an essential coenzyme for glucose-6-phosphate dehydrogenase which catalyzes the oxidation of glucose-6-phosphate to 6-phosphogluconic acid. This reaction initiates metabolism of glucose by a pathway other than the citric acid cycle. This route is known as the hexose phosphate shunt or phosphogluconate pathway. Other enzymes which utilize NADP as a coenzyme are: Alcohol dehydrogenase:NADP dependent; Aromatic ADH:NADP dependent; Ferredoxin-NADP reductase; L-Fucose dehydrogenase; Gabase; Galactose-1-phosphate uridyl transferase; Glucose dehydrogenase; L-Glutamic dehydrogenase; Glycerol dehydrogenase:NADP specific; Isocitric dehydrogenase; Malic enzymes; 5,10-Methylenetetrahydrofolate dehydrogenase; 6-Phosphogluconate dehydrogenase and Succinic semialdehyde dehydrogenase.

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